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Post-translational Modification: Ubiquitination, Thesis of Techniques and Instrumentation for Biochemistry

Bath Spa UniversityTechniques and Instrumentation for Biochemistry

Ubiquitination is a post-translational protein modification involving the attachment of ubiquitin, a 8.5 kda polypeptide, to the ε-amino group of lysine residues in target proteins. Monoubiquitination can lead to polyubiquitination, which targets proteins for degradation by the 26s proteasome. Ubiquitin is then recycled for reuse.

Typology: Thesis

2015/2016

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post translational modification ubiquitination
Ubiquitin is an about 8.5 kDa polypeptide consisting of 76 amino acids that is
appended to the 8 5 1 A-NH2 of lysine in target proteins via the C-terminal glycine of
ubiquitin. Following an initial monoubiquitination event, the formation of a
ubiquitin polymer may occur, and polyubiquitinated proteins are then recognized
by the 26S proteasome that catalyzes the degradation of the ubiquitinated protein
and the recycling of ubiquitin.
More information:
contact@creative-proteomics.com
Tel:5166698109

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post translational modification ubiquitination Ubiquitin is an about 8.5 kDa polypeptide consisting of 76 amino acids that is appended to the 8 5 1 A-NH2 of lysine in target proteins via the C-terminal glycine of ubiquitin. Following an initial monoubiquitination event, the formation of a ubiquitin polymer may occur, and polyubiquitinated proteins are then recognized by the 26S proteasome that catalyzes the degradation of the ubiquitinated protein and the recycling of ubiquitin. More information: contact@creative-proteomics.com Tel: